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Merck

907391

Sigma-Aldrich

Fmoc-L-photo-leucine

≥98%

Sinónimos:

(S)-2-(((9H-Fluoren-9-yl)methoxy)carbonylamino)-3-(3-methyl-3H-diazirin-3-yl)propanoic acid, (S)-2-(Fmoc-amino)-3-(3H-diazirin-3-yl)butanoic acid, Photo-Leu, Photo-crosslinking amino acid, Photoprobe building block

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About This Item

Fórmula empírica (notación de Hill):
C20H19N3O4
Número de CAS:
Peso molecular:
365.38
UNSPSC Code:
12352209
NACRES:
NA.22

assay

≥98%

form

powder

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

application(s)

peptide synthesis

functional group

Fmoc

storage temp.

2-8°C

Application

Fmoc-L-Photo-Leucine is a diazirine-containing, Fmoc-protected leucine amino acid and multifunctional photo-crosslinker. Its incorporation into peptides or small-molecule probes and tools allows for photoaffinity labeling of cellular targets and protein-protein interactions upon UV light (∼360 nm) irradiation to form a covalent bond. This and other multifunctional probe building blocks will continue to accelerate drug discovery research for probing cellular mechanisms, target ID/validation, and understanding traditionally undruggable targets. An unprotected version is also available as 907278.

Product can be used with our line of photoreactors: Including Penn PhD (Z744035) & SynLED 2.0 (Z744080)

related product

Referencia del producto
Descripción
Precios

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Aleš Marek et al.
Journal of the American Society for Mass Spectrometry, 25(5), 778-789 (2014-02-20)
Gas-phase dissociations were investigated for several peptide ions containing the Gly-Leu* N-terminal motif where Leu* was a modified norleucine residue containing the photolabile diazirine ring. Collisional activation of gas-phase peptide cations resulted in facile N₂ elimination that competed with backbone
Benjamin van der Meijden et al.
Journal of peptide science : an official publication of the European Peptide Society, 21(3), 231-235 (2015-02-03)
The antimicrobial activity of polymyxins against Gram-negative bacteria has been known for several decades, but the mechanism of action leading to cell death has not been fully explored. A key step after binding of the antibiotic to lipopolysaccharide (LPS) exposed
En-Wei Lin et al.
Bioconjugate chemistry, 25(10), 1902-1909 (2014-10-16)
A photoactivated, site-selective conjugation of poly(ethylene glycol) (PEG) to the glutathione (GSH) binding pocket of glutathione S-transferase (GST) is described. To achieve this, a GSH analogue (GSH-BP) was designed and chemically synthesized with three functionalities: (1) the binding affinity of
Jay M Janz et al.
Journal of the American Chemical Society, 133(40), 15878-15881 (2011-09-13)
Cell surface heptahelical G protein-coupled receptors (GPCRs) mediate critical cellular signaling pathways and are important pharmaceutical drug targets. (1) In addition to traditional small-molecule approaches, lipopeptide-based GPCR-derived pepducins have emerged as a new class of pharmaceutical agents. (2, 3)
Tangpo Yang et al.
Chemical science, 6(2), 1011-1017 (2015-02-01)
Post translational modifications (PTMs, e.g., phosphorylation, acetylation and methylation) of histone play important roles in regulating many fundamental cellular processes such as gene transcription, DNA replication and damage repair. While 'writer' and 'eraser' enzymes modify histones by catalyzing the addition

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